Different strategies to co-immobilize dextransucrase and dextranase onto agarose based supports: Operational stability study

Silva, Rhonyele Maciel da; Gonçalves, Luciana Rocha Barros; Rodrigues, Suelí

doi:10.1016/j.ijbiomac.2020.04.077

Cited by 8 publications

(2 citation statements)

References 58 publications

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“…Immobilized enzymes should be evaluated for operational stability in order to verify their application potential. The possibility of reuse minimizes costs in bioprocesses [62] and consolidates the stability of the immobilized enzyme [63]. Operational stability data for IBs are showed in Figure 5.…”

Section: Operational Stabilitymentioning

confidence: 97%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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In the present work the radish (Raphanus sativus L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies—immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications.

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Section: Operational Stabilitymentioning

confidence: 97%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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“…The matrices or supports for this novel technology can be categorised into the following: organic and inorganic compounds. The most reported enzyme supports of organic materials are organic membrane [76], chitosan [77,78], alginate [54], resin [79], collagen [80], gelatine [81], dextran [82], starch [83], carrageenan [42], agarose [84], protein [85], cellulose [86], activated carbon [87], agar [88], and chitin [89]. Synthetic organic materials are polyvinyl alcohol [90], polyurethane foam [91], polyacrylonitrile [92], polyethylene, polypropylene membrane, and polyacrylamide [93][94][95].…”

Section: Overview Of the Enzyme Carriers Materialsmentioning

confidence: 99%

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Mohidem,

Mohamad,

Rashid

et al. 2023

J. Compos. Sci.

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For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplifying downstream processing. This technology protects the enzyme from degradation or inactivation by harsh reaction conditions, making it more robust and suitable to be used in various applications. Recent strategies of immobilisation methods, such as adsorption, cross-linking, entrapment or encapsulation, and covalent bonding, were critically reviewed. These strategies have shown promising results in improving enzyme stability, activity, and reusability in various applications. A recent development in enzyme immobilisation in nanomaterials and agrowaste renewable carriers is underlined in the current review. Furthermore, the use of nanomaterials and agrowaste carriers in enzyme immobilisation has gained significant attention due to their unique properties, such as high surface area, high mass transfer, biocompatibility, and sustainability. These materials offer promising outcomes for developing more efficient and sustainable immobilised enzymes. This state-of-the-art strategy allows for better control over enzyme reactions and enhances their reusability, leading to more cost-effective and environmentally friendly processes. The use of renewable materials also helps to reduce waste generation and promote the utilisation of renewable resources, further contributing to the development of a circular economy.

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Exploration of a three-dimensional matrix as micro-reactor in the form of reactive polyaminosaccharide hydrogel beads using multipoint covalent interaction approach

2022

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Different strategies to co-immobilize dextransucrase and dextranase onto agarose based supports: Operational stability study

Cited by 8 publications

References 58 publications

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Exploration of a three-dimensional matrix as micro-reactor in the form of reactive polyaminosaccharide hydrogel beads using multipoint covalent interaction approach

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